The sequence of the alpha-subunit of the pea lectin has already been determined. We are proceeding with sequence studies on the beta-subunit which contains regions responsible for metal ion binding and the carbohydrate binding site. As in the case of the alpha-subunit, this sequence will be compared to the homologous region of Concanavalin A to further our understanding of lectin structure and function. Further, we will study the conformation of cholesterol in membranes and LDL using 13C-labeled materials and specialized NMR techniques (e.g.-high spin at the "magic angle"). This will be done in association with Drs. Ellis and Gruenstein. Preliminary studies have been initiated using a variety of growth conditions for human fibroblasts (e.g. free cholesterol, LDL, HDL) as well as studies with diseased cell lines. Finally, we will continue our studies of Concanavalin A with respect to the kinetics and thermodynamics of the unfolding and refolding process using a combination of fluorescence (MUM binding) and C. D. techniques.